79847
Hydroxynitrile Lyase, Arabidopsis thaliana, recombinant from E. coli
≥500 U/mL
Synonym(s):
Hydroxymandelonitrile Lyase, Arabidopsis thaliana, recombinant from E. coli
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About This Item
Specific activity:
≥500 U/mL
Recombinant:
expressed in E. coli
recombinant
expressed in E. coli
form
liquid
specific activity
≥500 U/mL
storage temp.
−20°C
Application
Hydroxynitrile lyases (Oxynitrilases) are used for various biotransformation processes and to convert a broad range of substrates. They may be used with bacterial nitrilases to generate biocatalysts .
Biochem/physiol Actions
Hydroxynitrile lyases (Oxynitrilases) catalyze the addition of HCN to aldehydes and ketones thereby forming α-hydroxynitriles, also known as cyanohydrins . Product 79847, Hydroxynitrile Lyase from Arabidopsis thaliana , is used to hydrolyze mandelonitrile.
Other Notes
1 U corresponds to the amount of enzyme which converts 1 μmol mandelonitrile per minte at pH 5.0 and 25°C.
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Storage Class
11 - Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
Regulatory Information
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White et al.
Plant physiology, 116(4), 1219-1225 (1998-04-29)
In the cyanogenic crop cassava (Manihot esculenta, Crantz), the final step in cyanide production is the conversion of acetone cyanohydrin, the deglycosylation product of linamarin, to cyanide plus acetone. This process occurs spontaneously at pH greater than 5. 0 or
Screening for hydroxynitrile lyases in plants
Hickel, A., Heinrich, G., et al.
Biotechnol. Tech., 11, 55-58 (1997)
Kathrin Emmi Scholz et al.
Applied and environmental microbiology, 78(14), 5025-5027 (2012-05-01)
Synthesis of chiral cyanohydrins is performed in a monophasic micro-aqueous reaction system using whole recombinant Escherichia coli cells expressing the Arabidopsis thaliana hydroxynitrile lyase (AtHNL). Microscopy studies employing a fusion of AtHNL with a flavin-based fluorescent protein (FbFP) reveal that
Stefanie Baum et al.
Applied and environmental microbiology, 78(1), 48-57 (2011-10-25)
The nitrilase from Pseudomonas fluorescens EBC191 converted 2-methyl-2-phenylpropionitrile, which contains a quaternary carbon atom in the α-position toward the nitrile group, and also similar sterically demanding substrates, such as 2-hydroxy-2-phenylpropionitrile (acetophenone cyanohydrin) or 2-acetyloxy-2-methylphenylacetonitrile. 2-Methyl-2-phenylpropionitrile was hydrolyzed to almost stoichiometric
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